@article { ISI:000334147300006,
	title = {Conformational transitions of cinnamoyl CoA reductase 1 from leucaena leucocephala},
	journal = {International Journal of Biological Macromolecules },
	volume = {64},
	year = {2014},
	month = {MAR},
	pages = {30-35},
	publisher = {ELSEVIER SCIENCE BV},
	type = {Article},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Conformational transitions of cinnamoyl CoA reductase, a key regulatory enzyme in lignin biosynthesis, from Leucaena leucocephala (L1-CCRH1) were studied using fluorescence and circular dichroism spectroscopy. The native protein possesses four trp residues exposed on the surface and 66\% of helical structure, undergoes rapid structural transitions at and above 45 C and starts forming aggregates at 55 C. LI-CCRH1 was transformed into acid induced (pH 2.0) molten globule like structure, exhibiting altered secondary structure, diminished tertiary structure and exposed hydrophobic residues. The molten globule like structure was examined for the thermal and chemical stability. The altered secondary structure of Ll -CCRH1 at pH 2.0 was stable up to 90 C. Also, in presence of 0.25 M guanidine hydrochloride (GdnHCI), it got transformed into different structure which was stable in the vicinity of 2 M GdnHCI (as compared to drastic loss of native structure in 2 M GdnHC1) as seen in far UV-CD spectra. The structural transition of LI-CCRH1 at pH 2.0 followed another transition after readjusting the pH to 8.0, forming a structure with hardly any similarity to that of native protein. (C) 2013 Elsevier B.V. All rights reserved.</p>},
	keywords = {Aggregation Cinnamoyl CoA reductase, Conformation, Molten globule, Thermostability, Unfolding},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2013.11.024},
	author = {Sonawane, Prashant D. and Khan, Bashir Mohammad and Gaikwad, Sushama M.}
}
@article { ISI:000369200500019,
	title = {Functional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera},
	journal = {International Journal of Biological Macromolecules},
	volume = {83},
	year = {2016},
	month = {FEB},
	pages = {160-170},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Functional and conformational transitions of mevalonate diphosphate decarboxylase (MDD), a key enzyme of mevalonate pathway in isoprenoid biosynthesis, from Bacopa monniera (BmMDD), cloned and overexpressed in Escherichia coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and Circular dichroism spectroscopy. Native BmMDD is a helix dominant structure with 45\% helix and 11\% sheets and possesses seven tryptophan residues with two residues exposed on surface, three residues partially exposed and two situated in the interior of the protein. Thermal denaturation of BmMDD causes rapid structural transitions at and above 40 degrees C and transient exposure of hydrophobic residues at 50 degrees C, leading to aggregation of the protein. An acid induced molten globule like structure was observed at pH 4, exhibiting altered but compact secondary structure, distorted tertiary structure and exposed hydrophobic residues. The molten globule displayed different response at higher temperature and similar response to chemical denaturation as compared to the native protein. The surface tryptophans have predominantly positively charged amino acids around them, as indicated by higher K-SV for IC as compared to that for CsCl. The native enzyme displayed two different lifetimes, vi (1.203 +/- 0.036 ns) and tau 2 (3.473 +/- 0.12 ns) indicating two populations of tryptophan. (C) 2015 Elsevier B.V. All rights reserved.</p>},
	keywords = {Aggregation, CD spectroscopy, Fluorescence quenching, Mevalonate diphosphate decarboxylase, Unfolding},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2015.11.067},
	author = {Shakeel, Abbassi and Patel, Krunal and Khan, Bashir Mohammad and Bhosale, Siddharth H. and Gaikwad, Sushama M.}
}
